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- PDB-9z9e: Structure of FabS1CE2_ER-3c in complex with the extracellular reg... -

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Basic information

Entry
Database: PDB / ID: 9z9e
TitleStructure of FabS1CE2_ER-3c in complex with the extracellular region of EGFR
Components
  • Epidermal growth factor receptor
  • heavy chain
  • light chain
KeywordsSIGNALING PROTEIN / epidermal growth factor receptor / high-affinity antibody / domain 3 / epidermal growth factor / inhibition
Function / homology
Function and homology information


multivesicular body, internal vesicle lumen / negative regulation of cardiocyte differentiation / Shc-EGFR complex / positive regulation of protein kinase C signaling / Inhibition of Signaling by Overexpressed EGFR / epidermal growth factor receptor activity / EGFR interacts with phospholipase C-gamma / epidermal growth factor binding / regulation of peptidyl-tyrosine phosphorylation / response to UV-A ...multivesicular body, internal vesicle lumen / negative regulation of cardiocyte differentiation / Shc-EGFR complex / positive regulation of protein kinase C signaling / Inhibition of Signaling by Overexpressed EGFR / epidermal growth factor receptor activity / EGFR interacts with phospholipase C-gamma / epidermal growth factor binding / regulation of peptidyl-tyrosine phosphorylation / response to UV-A / ubiquitin-dependent endocytosis / PLCG1 events in ERBB2 signaling / morphogenesis of an epithelial fold / PTK6 promotes HIF1A stabilization / ERBB2 Activates PTK6 Signaling / digestive tract morphogenesis / ERBB2-EGFR signaling pathway / Signaling by EGFR / eyelid development in camera-type eye / intracellular vesicle / cerebral cortex cell migration / ERBB2 Regulates Cell Motility / Developmental Lineage of Mammary Gland Myoepithelial Cells / protein insertion into membrane / protein tyrosine kinase activator activity / Signaling by ERBB4 / Respiratory syncytial virus (RSV) attachment and entry / negative regulation of epidermal growth factor receptor signaling pathway / PI3K events in ERBB2 signaling / hair follicle development / positive regulation of phosphorylation / positive regulation of peptidyl-serine phosphorylation / MAP kinase kinase kinase activity / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / embryonic placenta development / GAB1 signalosome / salivary gland morphogenesis / xenobiotic transport / positive regulation of G1/S transition of mitotic cell cycle / positive regulation of epidermal growth factor receptor signaling pathway / Signaling by ERBB2 / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / transmembrane receptor protein tyrosine kinase activity / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / EGFR Transactivation by Gastrin / epithelial cell proliferation / GRB2 events in ERBB2 signaling / SHC1 events in ERBB2 signaling / basal plasma membrane / ossification / cellular response to epidermal growth factor stimulus / positive regulation of DNA replication / positive regulation of epithelial cell proliferation / positive regulation of DNA repair / Signal transduction by L1 / positive regulation of protein localization to plasma membrane / cellular response to estradiol stimulus / phosphatidylinositol 3-kinase/protein kinase B signal transduction / cellular response to amino acid stimulus / sperm end piece / NOTCH3 Activation and Transmission of Signal to the Nucleus / clathrin-coated endocytic vesicle membrane / Signaling by ERBB2 TMD/JMD mutants / EGFR downregulation / receptor protein-tyrosine kinase / Constitutive Signaling by EGFRvIII / negative regulation of protein catabolic process / cell-cell adhesion / Signaling by ERBB2 ECD mutants / Signaling by ERBB2 KD Mutants / positive regulation of protein phosphorylation / positive regulation of miRNA transcription / positive regulation of fibroblast proliferation / cell morphogenesis / epidermal growth factor receptor signaling pathway / ruffle membrane / kinase binding / Downregulation of ERBB2 signaling / Constitutive Signaling by Aberrant PI3K in Cancer / neuron differentiation / HCMV Early Events / actin filament binding / cell junction / transmembrane signaling receptor activity / PIP3 activates AKT signaling / positive regulation of canonical Wnt signaling pathway / Cargo recognition for clathrin-mediated endocytosis / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / Clathrin-mediated endocytosis / ATPase binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / sperm principal piece / virus receptor activity / RAF/MAP kinase cascade / positive regulation of cell growth / protein tyrosine kinase activity / double-stranded DNA binding / sperm midpiece / early endosome membrane
Similarity search - Function
: / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain ...: / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain / Furin-like repeat / Furin-like repeats / Growth factor receptor cysteine-rich domain superfamily / : / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
: / DI(HYDROXYETHYL)ETHER / TRIETHYLENE GLYCOL / THIOCYANATE ION / Epidermal growth factor receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsSinger, A.U. / Mallette, E. / Bruce, H.A. / Blazer, L.L. / Adams, J.J. / Suits, M.D.L. / Sidhu, S.S.
Funding support Canada, 2items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR)MOP-93725 Canada
Canadian Institutes of Health Research (CIHR)MOP-136944 Canada
CitationJournal: Protein Sci. / Year: 2026
Title: Dual targeting of inhibitory EGFR epitopes with synthetic antibodies in therapeutic-resistant cancers.
Authors: Adams, J.J. / Mallette, E. / London, M. / Liang, R.J. / van Dyk, D. / Pavlovic, Z. / Pot, I. / Geyer, C.R. / Bruce, H.A. / Blazer, L.L. / Hokanson, C.A. / Suits, M.D.L. / Singer, A.U. / Sidhu, S.S.
History
DepositionNov 18, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 3, 2026Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Epidermal growth factor receptor
D: heavy chain
E: light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,64643
Polymers117,0293
Non-polymers4,61740
Water4,522251
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)101.060, 72.116, 126.211
Angle α, β, γ (deg.)90.000, 101.650, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Epidermal growth factor receptor / Proto-oncogene c-ErbB-1 / Receptor tyrosine-protein kinase erbB-1


Mass: 69133.773 Da / Num. of mol.: 1 / Mutation: residues 25-645
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EGFR, ERBB, ERBB1, HER1 / Plasmid: PSCSTA
Details (production host): N-terminal trypsinogen-2 signal peptide and a C-terminal thrombin cleavage site followed by a hexahistidine tag
Cell line (production host): Expi293 / Production host: Homo sapiens (human)
References: UniProt: P00533, receptor protein-tyrosine kinase

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Antibody , 2 types, 2 molecules DE

#2: Antibody heavy chain


Mass: 24696.559 Da / Num. of mol.: 1 / Mutation: K127Q and E158G
Source method: isolated from a genetically manipulated source
Details: FAB PRODUCED BY RANDOMIZATION OF CDR REGIONS AND SELECTED BY PHAGE DISPLAY.
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PSDCSTA / Cell line (production host): Expi293 / Production host: Homo sapiens (human)
#3: Antibody light chain


Mass: 23198.660 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PSCSTA / Cell line (production host): Expi293 / Production host: Homo sapiens (human)

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Sugars , 3 types, 6 molecules

#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#5: Polysaccharide alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1235.105 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-2DManpa1-3[DManpa1-3DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-f1_d2-e1_f3-g1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#6: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 8 types, 285 molecules

#7: Chemical
ChemComp-SCN / THIOCYANATE ION


Mass: 58.082 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: CNS
#8: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Cl
#9: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: Na
#10: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: K
#11: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C4H10O3
#12: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O4
#13: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#14: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 251 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.85 Å3/Da / Density % sol: 68.04 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop
Details: 0.2M potassium thiocyanate, 20% PEG3350, cryoprotected with this buffer plus 30% ethylene glycol
Temp details: room temperature

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSLS-II / Beamline: 17-ID-2 / Wavelength: 0.979346 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Feb 1, 2025 / Details: mirrors
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979346 Å / Relative weight: 1
ReflectionResolution: 2.4→43.112 Å / Num. obs: 66379 / % possible obs: 95.1 % / Redundancy: 4.3 % / Biso Wilson estimate: 40.33 Å2 / CC1/2: 0.988 / Rmerge(I) obs: 0.13 / Rpim(I) all: 0.106 / Rrim(I) all: 0.168 / Net I/σ(I): 7.9
Reflection shellResolution: 2.4→2.443 Å / Redundancy: 4.5 % / Rmerge(I) obs: 1.24 / Mean I/σ(I) obs: 1.2 / Num. unique obs: 3445 / CC1/2: 0.364 / Rpim(I) all: 1.029 / Rrim(I) all: 1.619 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
PHENIX1.20.1_4487refinement
autoPROCdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→43.11 Å / SU ML: 0.3167 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.2485
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2426 3286 4.95 %
Rwork0.1945 63045 -
obs0.1969 66331 95.07 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 58.85 Å2
Refinement stepCycle: LAST / Resolution: 2.4→43.11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7883 0 281 251 8415
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0098375
X-RAY DIFFRACTIONf_angle_d1.054511359
X-RAY DIFFRACTIONf_chiral_restr0.06611308
X-RAY DIFFRACTIONf_plane_restr0.00881457
X-RAY DIFFRACTIONf_dihedral_angle_d17.41063059
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.440.33451530.30942808X-RAY DIFFRACTION99.53
2.44-2.480.34341480.30982890X-RAY DIFFRACTION99.74
2.48-2.520.35381330.30332849X-RAY DIFFRACTION99.83
2.52-2.560.30331470.29222869X-RAY DIFFRACTION99.8
2.56-2.610.30051340.26982862X-RAY DIFFRACTION99.93
2.61-2.650.32891310.26562674X-RAY DIFFRACTION95.96
2.68-2.710.2782860.25761718X-RAY DIFFRACTION93.57
2.71-2.770.29921430.25572887X-RAY DIFFRACTION99.87
2.77-2.830.26371630.23682815X-RAY DIFFRACTION99.83
2.83-2.90.31281530.24612903X-RAY DIFFRACTION100
2.9-2.980.3211740.23312843X-RAY DIFFRACTION100
2.98-3.070.2571620.2182823X-RAY DIFFRACTION99.87
3.07-3.170.26961580.20952895X-RAY DIFFRACTION99.97
3.17-3.280.23311240.20062906X-RAY DIFFRACTION100
3.28-3.410.24961340.19522840X-RAY DIFFRACTION98.44
3.45-3.570.25861180.19382087X-RAY DIFFRACTION98.48
3.57-3.760.22271150.19022247X-RAY DIFFRACTION77.24
3.76-3.990.25321340.16722522X-RAY DIFFRACTION87.14
3.99-4.30.20011440.14932876X-RAY DIFFRACTION100
4.3-4.730.17081540.12432895X-RAY DIFFRACTION100
4.73-5.420.18411560.14152901X-RAY DIFFRACTION99.9
5.42-6.820.18721720.18062914X-RAY DIFFRACTION99.94
6.82-43.110.24821500.1793021X-RAY DIFFRACTION99.87
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
14.44778645375-1.41315939594-0.7391764459243.896964679420.1620570202613.026235299240.4615061250650.9648775174710.0461891544632-0.612377330096-0.5004962308910.19482962609-0.395894762679-1.019612474080.04329023743470.5597247159680.2204863503480.03729897702180.858486139187-0.04761858352950.5191835543-27.4853996519-6.64709191757-48.0865359237
25.26795995554-0.327298754049-0.3876410321820.923888097871-0.266127538598-0.319738045101-0.0687600766873-0.900338767593-0.03738295883960.0026666409275-0.10410957973-0.4355118635110.01035878789150.3076004364530.1591993695030.4719320771390.07862321888250.03126329105430.6007212638020.005405752051170.666829045805-11.9861192116-12.4576988598-28.7295812724
33.111258872350.4209567559720.8286491719992.840952663550.7377754474151.25513673581-0.0458896786141-0.6167223700340.107826737739-0.03684947711590.161837660646-0.568785307197-0.04548677596730.254405623393-0.08644059470090.2200457406360.08548971154880.04544668893030.696922470375-0.1159310182830.356729974908-39.5324920564.28397726005-12.0290333279
49.29961657255-5.562029277860.09578690280823.583668711140.6472933132791.46755890656-0.0904740811054-0.7371172240641.124428775760.4464006370030.0681821070395-0.01839033226370.0753880708257-0.322255016784-0.03636660240250.342738252719-0.04431156519180.1012474905230.9280226429080.04117978613070.8715225473517.15655504059-1.93665681605-11.5907744023
51.483160104020.5130066034880.5266968064441.455587789720.09903042489893.05413164046-0.0456078676239-0.221689604179-0.20718500954-0.4422711214190.01337434688850.136481726170.224417921578-0.1245105435460.03346731445030.2978367561260.0284550440733-0.0536183693380.2308828360150.01636805750290.290336696266-70.6808799486-10.1028934687-29.6267423205
61.392234507320.03748974162420.9192981139870.1638821069831.025804213032.005935044580.13215211111-0.034043037052-0.0252298306539-0.118760383371-0.1037306844840.08177528363230.240970490647-0.03469871039280.02627445503380.463239436907-0.0328101001623-0.05317747547420.1778511639190.0521084048790.375989241128-78.6974576386-0.0225040030533-49.0556120683
72.186540501470.493981459026-0.3139247056721.253547914630.9726792360892.708440289550.3850915822280.309950322942-0.122028031755-0.238804427472-0.187773187909-0.05261621015420.00582961730914-0.101591910589-0.06004814389080.5529119471430.0593180092503-0.1034369972110.2378504115030.03343074388760.433029872262-82.30697796550.380162013233-65.7940983562
81.10403951854-0.1367743138770.4285992250882.15759677882-0.1787623052491.35425222906-0.39030914368-0.2671554199280.48566200755-0.2789746695820.1572860900830.466645813256-0.363400989488-0.0849817689994-0.0801691471780.361322862994-0.00591903020325-0.1589633259170.318875618677-0.05305511106550.476643154075-68.225419738513.0377970103-29.1302165037
91.23689183621-0.01108488495461.705309664780.224075719088-0.4304799485132.12811073601-0.320660461718-0.1942505075980.558695310677-0.1756130662850.1989830990840.247633613047-0.360906178570.1310181011590.158357563690.477908594681-0.00586073891099-0.1440947519870.270264022719-0.0403780153980.520470910858-70.475193650214.6885118076-32.443923069
101.781985347060.746434139033-0.1666228294265.930087739491.365766800872.993318884360.264762312611-0.223746201962-0.3737181293050.0932555858552-0.3508976290510.170408706481-0.151571495561-0.3064989371190.09211894907650.4697525085350.00512456758855-0.125647688030.1695285513890.05472733339530.410922856961-91.835326429711.0072830405-57.7445710329
110.197624562847-0.1456877299610.1010564499523.41648719066-0.2690473051671.114974354820.0663927189532-0.1030344955840.820592822580.501760637628-0.192223237963-0.275716304642-0.42039960105-0.02488785834540.02634991059590.550599336064-0.111585505803-0.05098842583090.190571262390.09042596767550.444032896068-86.776645701713.3102789545-51.6727594255
123.626394130214.00060634226-0.4298635507594.44957437508-0.3349629848940.4528814019190.282724739919-0.122731448143-0.1816653026940.391952253816-0.461161160279-0.0105400748508-0.39503325192-0.0477139619376-0.4924799500080.12141590265-0.500731166315-0.0791434201331-0.9346524052610.1046520321970.399356288659-100.8241512475.53275561867-57.6431494162
131.71713661785-0.924323773264-1.394554559080.8792244316890.5186096258221.71062406392-0.2284477177910.2078307442480.05903874268840.02795869962190.05230933674630.368117103728-0.338832155819-0.287094837312-0.6465623526180.558501115438-0.00636823428919-0.1800155803080.2244307977310.06151894346350.379859369588-97.773291397117.4540268986-60.6624083892
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'A' and (resid 4 through 197 )AA4 - 1971 - 194
22chain 'A' and (resid 198 through 321 )AA198 - 321195 - 312
33chain 'A' and (resid 322 through 523 )AA322 - 523313 - 514
44chain 'A' and (resid 524 through 614 )AA524 - 614515 - 604
55chain 'D' and (resid 1 through 100 )DR1 - 1001 - 100
66chain 'D' and (resid 101 through 185 )DR101 - 185101 - 185
77chain 'D' and (resid 186 through 226 )DR186 - 226186 - 226
88chain 'E' and (resid 1 through 61 )EZ1 - 611 - 61
99chain 'E' and (resid 62 through 113 )EZ62 - 11362 - 113
1010chain 'E' and (resid 114 through 150 )EZ114 - 150114 - 150
1111chain 'E' and (resid 151 through 174 )EZ151 - 174151 - 174
1212chain 'E' and (resid 175 through 188 )EZ175 - 188175 - 188
1313chain 'E' and (resid 189 through 212 )EZ189 - 212189 - 212

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